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Database: UniProt
Entry: P62333
LinkDB: P62333
Original site: P62333 
ID   PRS10_HUMAN             Reviewed;         389 AA.
AC   P62333; B2R975; P49719; Q6IBU3; Q92524;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-JUN-2021, entry version 181.
DE   RecName: Full=26S proteasome regulatory subunit 10B;
DE   AltName: Full=26S proteasome AAA-ATPase subunit RPT4;
DE   AltName: Full=Proteasome 26S subunit ATPase 6;
DE   AltName: Full=Proteasome subunit p42;
GN   Name=PSMC6; Synonyms=SUG2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Aorta;
RX   PubMed=8674546; DOI=10.1016/0014-5793(96)00489-9;
RA   Fujiwara T., Watanabe T.K., Tanaka K., Slaughter C.A., Demartino G.N.;
RT   "cDNA cloning of p42, a shared subunit of two proteasome regulatory
RT   proteins, reveals a novel member of the AAA protein family.";
RL   FEBS Lett. 387:184-188(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Li Y., Benezra R.;
RT   "Human SUG2.";
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Caudate nucleus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Urinary bladder;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8621709; DOI=10.1074/jbc.271.6.3112;
RA   Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X.,
RA   Hisamatsu H., Tanaka K., Slaughter C.A.;
RT   "Identification, purification, and characterization of a PA700-dependent
RT   activator of the proteasome.";
RL   J. Biol. Chem. 271:3112-3118(1996).
RN   [9]
RP   FUNCTION.
RX   PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
RA   Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N., Yoshimura T.,
RA   Tanaka K., Ichihara A.;
RT   "Demonstration that a human 26S proteolytic complex consists of a
RT   proteasome and multiple associated protein components and hydrolyzes ATP
RT   and ubiquitin-ligated proteins by closely linked mechanisms.";
RL   Eur. J. Biochem. 206:567-578(1992).
RN   [10]
RP   INTERACTION WITH PAAF1.
RX   PubMed=15831487; DOI=10.1128/mcb.25.9.3842-3853.2005;
RA   Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT   "Proteasomal ATPase-associated factor 1 negatively regulates proteasome
RT   activity by interacting with proteasomal ATPases.";
RL   Mol. Cell. Biol. 25:3842-3853(2005).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17323924; DOI=10.1021/bi061994u;
RA   Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT   "Mass spectrometric characterization of the affinity-purified human 26S
RT   proteasome complex.";
RL   Biochemistry 46:3553-3565(2007).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-72 AND LYS-206, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [17]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-440, AND SUBUNIT.
RX   PubMed=27428775; DOI=10.1038/nsmb.3273;
RA   Huang X., Luan B., Wu J., Shi Y.;
RT   "An atomic structure of the human 26S proteasome.";
RL   Nat. Struct. Mol. Biol. 23:778-785(2016).
RN   [18]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS) OF 1-440, AND SUBUNIT.
RX   PubMed=27342858; DOI=10.1073/pnas.1608050113;
RA   Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
RA   Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
RT   "Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
CC   -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       This complex plays a key role in the maintenance of protein homeostasis
CC       by removing misfolded or damaged proteins, which could impair cellular
CC       functions, and by removing proteins whose functions are no longer
CC       required. Therefore, the proteasome participates in numerous cellular
CC       processes, including cell cycle progression, apoptosis, or DNA damage
CC       repair. PSMC6 belongs to the heterohexameric ring of AAA (ATPases
CC       associated with diverse cellular activities) proteins that unfolds
CC       ubiquitinated target proteins that are concurrently translocated into a
CC       proteolytic chamber and degraded into peptides.
CC       {ECO:0000269|PubMed:1317798}.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC       regulatory subunits (RP). The regulatory particle is made of a lid
CC       composed of 9 subunits, a base containing 6 ATPases including PSMC6 and
CC       few additional components (PubMed:27428775, PubMed:27342858). Interacts
CC       with PAAF1 (PubMed:15831487). {ECO:0000269|PubMed:15831487,
CC       ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
CC   -!- INTERACTION:
CC       P62333; Q13895: BYSL; NbExp=3; IntAct=EBI-357669, EBI-358049;
CC       P62333; Q8TAB5: C1orf216; NbExp=4; IntAct=EBI-357669, EBI-747505;
CC       P62333; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-357669, EBI-10247802;
CC       P62333; Q16543: CDC37; NbExp=3; IntAct=EBI-357669, EBI-295634;
CC       P62333; P46108: CRK; NbExp=10; IntAct=EBI-357669, EBI-886;
CC       P62333; P46109: CRKL; NbExp=5; IntAct=EBI-357669, EBI-910;
CC       P62333; Q6BCY4: CYB5R2; NbExp=3; IntAct=EBI-357669, EBI-744761;
CC       P62333; P22607: FGFR3; NbExp=3; IntAct=EBI-357669, EBI-348399;
CC       P62333; Q14957: GRIN2C; NbExp=3; IntAct=EBI-357669, EBI-8285963;
CC       P62333; P52655: GTF2A1; NbExp=3; IntAct=EBI-357669, EBI-389518;
CC       P62333; P04792: HSPB1; NbExp=3; IntAct=EBI-357669, EBI-352682;
CC       P62333; P62191: PSMC1; NbExp=7; IntAct=EBI-357669, EBI-357598;
CC       P62333; P17980: PSMC3; NbExp=16; IntAct=EBI-357669, EBI-359720;
CC       P62333; P43686: PSMC4; NbExp=5; IntAct=EBI-357669, EBI-743997;
CC       P62333; P62195: PSMC5; NbExp=14; IntAct=EBI-357669, EBI-357745;
CC       P62333; P62333: PSMC6; NbExp=4; IntAct=EBI-357669, EBI-357669;
CC       P62333; O00233: PSMD9; NbExp=15; IntAct=EBI-357669, EBI-750973;
CC       P62333; O00560: SDCBP; NbExp=6; IntAct=EBI-357669, EBI-727004;
CC       P62333; O43304: SEC14L5; NbExp=3; IntAct=EBI-357669, EBI-12224055;
CC       P62333; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-357669, EBI-455078;
CC       P62333; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-357669, EBI-10180829;
CC       P62333; O76024: WFS1; NbExp=3; IntAct=EBI-357669, EBI-720609;
CC       P62333; P59595: N; Xeno; NbExp=3; IntAct=EBI-357669, EBI-7602718;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC   -!- CAUTION: Alternative initiation from an upstream conserved methionine
CC       cannot be fully excluded but is not experimentally supported while
CC       initiation from the displayed methionine is supported by
CC       PubMed:17323924. {ECO:0000305}.
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DR   EMBL; D78275; BAA11338.1; -; mRNA.
DR   EMBL; AF006305; AAB61616.1; -; mRNA.
DR   EMBL; BT006843; AAP35489.1; -; mRNA.
DR   EMBL; CR456709; CAG32990.1; -; mRNA.
DR   EMBL; AK313670; BAG36422.1; -; mRNA.
DR   EMBL; CH471078; EAW65645.1; -; Genomic_DNA.
DR   EMBL; BC005390; AAH05390.1; -; mRNA.
DR   CCDS; CCDS9710.2; -.
DR   PIR; S71316; S71316.
DR   RefSeq; NP_002797.3; NM_002806.3.
DR   PDB; 5GJQ; EM; 4.50 A; L=1-389.
DR   PDB; 5GJR; EM; 3.50 A; L/z=1-389.
DR   PDB; 5L4G; EM; 4.02 A; L=1-389.
DR   PDB; 5LN3; EM; 6.80 A; L=1-389.
DR   PDB; 5M32; EM; 3.80 A; f=1-379.
DR   PDB; 5T0C; EM; 3.80 A; AE/BE=1-389.
DR   PDB; 5T0G; EM; 4.40 A; E=1-389.
DR   PDB; 5T0H; EM; 6.80 A; E=1-389.
DR   PDB; 5T0I; EM; 8.00 A; E=1-389.
DR   PDB; 5T0J; EM; 8.00 A; E=1-389.
DR   PDB; 5VFP; EM; 4.20 A; E=15-389.
DR   PDB; 5VFQ; EM; 4.20 A; E=15-389.
DR   PDB; 5VFR; EM; 4.90 A; E=15-389.
DR   PDB; 5VFS; EM; 3.60 A; E=1-389.
DR   PDB; 5VFT; EM; 7.00 A; E=37-389.
DR   PDB; 5VFU; EM; 5.80 A; E=37-389.
DR   PDB; 5VGZ; EM; 3.70 A; E=11-114.
DR   PDB; 5VHF; EM; 5.70 A; E=11-389.
DR   PDB; 5VHH; EM; 6.10 A; E=11-389.
DR   PDB; 5VHI; EM; 6.80 A; E=11-389.
DR   PDB; 5VHJ; EM; 8.50 A; E=128-389.
DR   PDB; 5VHM; EM; 8.30 A; E=128-389.
DR   PDB; 5VHN; EM; 7.30 A; E=115-389.
DR   PDB; 5VHO; EM; 8.30 A; E=128-389.
DR   PDB; 5VHP; EM; 7.90 A; E=128-389.
DR   PDB; 5VHQ; EM; 8.90 A; E=128-389.
DR   PDB; 5VHR; EM; 7.70 A; E=128-389.
DR   PDB; 5VHS; EM; 8.80 A; E=11-389.
DR   PDB; 6MSB; EM; 3.00 A; E=1-389.
DR   PDB; 6MSD; EM; 3.20 A; E=1-389.
DR   PDB; 6MSE; EM; 3.30 A; E=1-389.
DR   PDB; 6MSG; EM; 3.50 A; E=1-389.
DR   PDB; 6MSH; EM; 3.60 A; E=1-389.
DR   PDB; 6MSJ; EM; 3.30 A; E=1-389.
DR   PDB; 6MSK; EM; 3.20 A; E=1-389.
DR   PDB; 6WJN; EM; 5.70 A; E=15-389.
DR   PDBsum; 5GJQ; -.
DR   PDBsum; 5GJR; -.
DR   PDBsum; 5L4G; -.
DR   PDBsum; 5LN3; -.
DR   PDBsum; 5M32; -.
DR   PDBsum; 5T0C; -.
DR   PDBsum; 5T0G; -.
DR   PDBsum; 5T0H; -.
DR   PDBsum; 5T0I; -.
DR   PDBsum; 5T0J; -.
DR   PDBsum; 5VFP; -.
DR   PDBsum; 5VFQ; -.
DR   PDBsum; 5VFR; -.
DR   PDBsum; 5VFS; -.
DR   PDBsum; 5VFT; -.
DR   PDBsum; 5VFU; -.
DR   PDBsum; 5VGZ; -.
DR   PDBsum; 5VHF; -.
DR   PDBsum; 5VHH; -.
DR   PDBsum; 5VHI; -.
DR   PDBsum; 5VHJ; -.
DR   PDBsum; 5VHM; -.
DR   PDBsum; 5VHN; -.
DR   PDBsum; 5VHO; -.
DR   PDBsum; 5VHP; -.
DR   PDBsum; 5VHQ; -.
DR   PDBsum; 5VHR; -.
DR   PDBsum; 5VHS; -.
DR   PDBsum; 6MSB; -.
DR   PDBsum; 6MSD; -.
DR   PDBsum; 6MSE; -.
DR   PDBsum; 6MSG; -.
DR   PDBsum; 6MSH; -.
DR   PDBsum; 6MSJ; -.
DR   PDBsum; 6MSK; -.
DR   PDBsum; 6WJN; -.
DR   SMR; P62333; -.
DR   BioGRID; 111679; 204.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P62333; -.
DR   DIP; DIP-38150N; -.
DR   IntAct; P62333; 104.
DR   MINT; P62333; -.
DR   STRING; 9606.ENSP00000401802; -.
DR   ChEMBL; CHEMBL2364701; -.
DR   iPTMnet; P62333; -.
DR   MetOSite; P62333; -.
DR   PhosphoSitePlus; P62333; -.
DR   SwissPalm; P62333; -.
DR   BioMuta; PSMC6; -.
DR   DMDM; 51702772; -.
DR   REPRODUCTION-2DPAGE; IPI00021926; -.
DR   EPD; P62333; -.
DR   jPOST; P62333; -.
DR   MassIVE; P62333; -.
DR   MaxQB; P62333; -.
DR   PaxDb; P62333; -.
DR   PeptideAtlas; P62333; -.
DR   PRIDE; P62333; -.
DR   ProteomicsDB; 57397; -.
DR   Antibodypedia; 23885; 294 antibodies.
DR   DNASU; 5706; -.
DR   Ensembl; ENST00000445930; ENSP00000401802; ENSG00000100519.
DR   GeneID; 5706; -.
DR   KEGG; hsa:5706; -.
DR   UCSC; uc059bor.1; human.
DR   CTD; 5706; -.
DR   DisGeNET; 5706; -.
DR   GeneCards; PSMC6; -.
DR   HGNC; HGNC:9553; PSMC6.
DR   HPA; ENSG00000100519; Low tissue specificity.
DR   MIM; 602708; gene.
DR   neXtProt; NX_P62333; -.
DR   OpenTargets; ENSG00000100519; -.
DR   PharmGKB; PA33898; -.
DR   VEuPathDB; HostDB:ENSG00000100519.11; -.
DR   eggNOG; KOG0651; Eukaryota.
DR   GeneTree; ENSGT01020000230346; -.
DR   HOGENOM; CLU_000688_2_2_1; -.
DR   InParanoid; P62333; -.
DR   OrthoDB; 571919at2759; -.
DR   PhylomeDB; P62333; -.
DR   TreeFam; TF106229; -.
DR   PathwayCommons; P62333; -.
DR   Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR   Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR   Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR   Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-HSA-202424; Downstream TCR signaling.
DR   Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR   Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-HSA-4641257; Degradation of AXIN.
DR   Reactome; R-HSA-4641258; Degradation of DVL.
DR   Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR   Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR   Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR   Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR   Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-HSA-5689603; UCH proteinases.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
DR   Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR   Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-69481; G2/M Checkpoints.
DR   Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR   Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR   Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; P62333; -.
DR   BioGRID-ORCS; 5706; 786 hits in 964 CRISPR screens.
DR   ChiTaRS; PSMC6; human.
DR   GeneWiki; PSMC6; -.
DR   GenomeRNAi; 5706; -.
DR   Pharos; P62333; Tbio.
DR   PRO; PR:P62333; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; P62333; protein.
DR   Bgee; ENSG00000100519; Expressed in endometrium and 117 other tissues.
DR   ExpressionAtlas; P62333; baseline and differential.
DR   Genevisible; P62333; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; TAS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0036402; F:proteasome-activating ATPase activity; IEA:InterPro.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IBA:GO_Central.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:UniProtKB.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   InterPro; IPR005937; 26S_Psome_P45-like.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB.
DR   InterPro; IPR035263; PSMC6.
DR   PANTHER; PTHR23073:SF76; PTHR23073:SF76; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Proteasome; Reference proteome.
FT   CHAIN           1..389
FT                   /note="26S proteasome regulatory subunit 10B"
FT                   /id="PRO_0000084732"
FT   NP_BIND         174..181
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         72
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         206
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CONFLICT        276
FT                   /note="I -> T (in Ref. 1; BAA11338)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   389 AA;  44173 MW;  B26421295742CACD CRC64;
     MADPRDKALQ DYRKKLLEHK EIDGRLKELR EQLKELTKQY EKSENDLKAL QSVGQIVGEV
     LKQLTEEKFI VKATNGPRYV VGCRRQLDKS KLKPGTRVAL DMTTLTIMRY LPREVDPLVY
     NMSHEDPGNV SYSEIGGLSE QIRELREVIE LPLTNPELFQ RVGIIPPKGC LLYGPPGTGK
     TLLARAVASQ LDCNFLKVVS SSIVDKYIGE SARLIREMFN YARDHQPCII FMDEIDAIGG
     RRFSEGTSAD REIQRTLMEL LNQMDGFDTL HRVKMIMATN RPDTLDPALL RPGRLDRKIH
     IDLPNEQARL DILKIHAGPI TKHGEIDYEA IVKLSDGFNG ADLRNVCTEA GMFAIRADHD
     FVVQEDFMKA VRKVADSKKL ESKLDYKPV
//
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